SML3678
ML-SI3
≥98% (HPLC)
Synonyme(s) :
N-[2-[4-(2-Methoxyphenyl)-1-piperazinyl]cyclohexyl]benzenesulfonamide
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About This Item
Produits recommandés
Niveau de qualité
Pureté
≥98% (HPLC)
Forme
powder
Couleur
white to beige
Solubilité
DMSO: 2 mg/mL, clear
Température de stockage
-10 to -25°C
Actions biochimiques/physiologiques
ML-SI3 is a 4-diastereomer racemate (2 cis and 2 trans isomers) with a cation channel TRPML1-blocking (IC50 = 3.1 μM/trans, 18.5 μM/cis against 5 μM ML-SA1-induced cellular calcium response) and TRPML2-activating activity (EC50 = 3.3 μM/trans, 9.4 μM/cis), while exhibiting much weaker TRPML3 potency (EC50 = 28.5 μM/trans, IC50 = 29.0 μM/cis). ML-SI3 is shown to compete against ML-SA1 for binding the same TRPML1 hydrophobic cavity. Comparing with ML-SI1 (GW405833), ML-SI3 is more potent and not agonist-dependent, effectively antagonizing against TRPML1 activation by both MK6-83 and ML-SA1.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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Developmental cell, 26(5), 511-524 (2013-09-03)
Phagocytosis of large extracellular particles such as apoptotic bodies requires delivery of the intracellular endosomal and lysosomal membranes to form plasmalemmal pseudopods. Here, we identified mucolipin TRP channel 1 (TRPML1) as the key lysosomal Ca2+ channel regulating focal exocytosis and
Structure (London, England : 1993), 29(11), 1295-1302 (2021-06-26)
Transient receptor potential mucolipin 1 (TRPML1) regulates lysosomal calcium signaling, lipid trafficking, and autophagy-related processes. This channel is regulated by phosphoinositides and the low pH environment of the lysosome, maintaining calcium levels essential for proper lysosomal function. Recently, several small
European journal of medicinal chemistry, 210, 112966-112966 (2020-11-15)
The members of the TRPML subfamily of non-selective cation channels (TRPML1-3) are involved in the regulation of important lysosomal and endosomal functions, and mutations in TRPML1 are associated with the neurodegenerative lysosomal storage disorder mucolipidosis type IV. For in-depth investigation
Proceedings of the National Academy of Sciences of the United States of America, 112(11), E1373-E1381 (2015-03-04)
Upon nutrient starvation, autophagy digests unwanted cellular components to generate catabolites that are required for housekeeping biosynthesis processes. A complete execution of autophagy demands an enhancement in lysosome function and biogenesis to match the increase in autophagosome formation. Here, we
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